Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Effects of Moisture Content on Non-Fracture Dynamic Properties and Fracture Quality of Pacific Whiting Surimi

  • Esturk, Okan (Department of Food Science and Technology, OSU Seafood Laboratory, Oregon State University) ;
  • Park, Jae-Won (Department of Food Science and Technology, OSU Seafood Laboratory, Oregon State University) ;
  • Raik, Moo-Yeol (Institute of Life Science and Resources, Department of Food Science and Biotechnology, Kyung Hee University) ;
  • Kim, Byung-Yong (Institute of Life Science and Resources, Department of Food Science and Biotechnology, Kyung Hee University)
  • Published : 2006.12.31
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Abstract

The effects of moisture content on non-fracture dynamic properties and fracture gel quality of Pacific whiting surimi were investigated to determine their relationships. Surimi samples were tested at various moisture contents (75, 78, and 81 %). Torsion test showed that shear stress decreased rapidly and strain values decreased gradually as moisture concentration increased. Dynamic storage modulus (G') also decreased as moisture content increased. A strong positive correlation ($R^2=0.90$ to 0.99) was found between the G' measured at temperatures between 10 and $45^{\circ}C$ and fracture stress values. The results indicate that dynamic rheological measurements could be used as a tool for early gel quality assessment.

Keywords

References

  1. Kim BY, Park Jw. Rheology and texture properties of surimi gels. pp. 491-582. In: Surimi and Surimi Seafood. 2nd ed. Park JW (ed). CRC, New York, NY, USA (2005)
  2. Lanier TC. Functional properties of surimi. Food Technol.-Chicago 40: 107-114 (1986)
  3. Lanier TC. Gelation chemistry. pp. 435-489. In: Surimi and Surimi Seafood. 20d ed. Park JW (ed). CRC, New York, NY, USA.(2005)
  4. Matsumoto JJ. Chemical deterioration of muscle proteins during frozen storage. pp. 95-124. In: Chemical Deterioration of Proteins. Whitaker JR, Fujimaki M (eds). Advances in Chemistry. Series No. 123. American Chemical Society, Washington, DC, USA (1980)
  5. Borderias AJ, Jimenez-Colmenero F, Tejada M. Parameters affecting viscosity as a quality control for frozen fish. Mar. Fish Rev. 47: 4345 (1985)
  6. Hamann DD, MacDonald GA. Rheology and texture properties of surimi and surimi-based Foods. pp. 429-500. In: Surimi Technology. Lanier TC, Lee CM (eds). Marcel Dekker Inc., New York, NY, USA (1992)
  7. Park JW, Yongsavadigul J, Lin TM. Rheological behavior and potential cross-linking of Pacific whiting (Merluccius productus) surimi gel. J Food Sci. 59: 773-776 (1994) https://doi.org/10.1111/j.1365-2621.1994.tb08125.x
  8. Hamann DD. Structural failure in foods. pp. 351-383. In: Physical Properties of Foods. Peleg M, Bagley E (eds). AVI Publishing Co., Westport, CT, USA (1983)
  9. Yoon WB, Park JW, Kim BY Linear programming in blending various components of surimi seafood. J. Food Sci 62: 561-567 (1997) https://doi.org/10.1111/j.1365-2621.1997.tb04430.x
  10. Reppond KD, Babbitt JK. Gel properties of surimi from various fish species as affected by moisture content. J. Food Sci. 62: 33-36 (1997) https://doi.org/10.1111/j.1365-2621.1997.tb04362.x
  11. Hamann DD. Rheology as a means of evaluating muscle functionality of processed foods. J. Food Technol. 42: 66-71 (1988)
  12. Ogawa M, Kanamaru J, Miyashita H, Tamiya T, Tsuchiya T. Alphahelical structure of fish actomyosin: changes during setting. J. Food Sci. 60: 297-299 (1995) https://doi.org/10.1111/j.1365-2621.1995.tb05659.x
  13. Stone AP, Stanley DW. Mechanism of fish muscle gelation. Food Res. Int. 25: 381-388 (1992) https://doi.org/10.1016/0963-9969(92)90113-J
  14. Sano T, Noguchi SF, Marsumoto JJ, Tsuchiya T. Thermal gelation characteristics of myosin subfragments. J. Food Sci. 55: 55-58, 70 (1990) https://doi.org/10.1111/j.1365-2621.1990.tb06015.x
  15. Mleko S, Foegeding EA. pH induced aggregation and weak gel formation of whey protein polymers. J. Food Sci. 65: 139-143 (2000) https://doi.org/10.1111/j.1365-2621.2000.tb15969.x